Iron in PDB 3h58: Myoglobin Cavity Mutant H64LV68N Met Form

The structure of Myoglobin Cavity Mutant H64LV68N Met Form, PDB code: 3h58 was solved by J.Soman, J.S.Olson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.03 / 1.80
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	90.130, 90.130, 45.260, 90.00, 90.00, 120.00
R / Rfree (%)	19.6 / 21.9

The binding sites of Iron atom in the Myoglobin Cavity Mutant H64LV68N Met Form (pdb code 3h58). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Myoglobin Cavity Mutant H64LV68N Met Form, PDB code: 3h58:

Iron binding site 1 out of 1 in the Myoglobin Cavity Mutant H64LV68N Met Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Myoglobin Cavity Mutant H64LV68N Met Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:7.6 occ:1.00 FE A:HEM154 0.0 7.6 1.0 ND A:HEM154 2.0 14.8 1.0 NA A:HEM154 2.0 14.8 1.0 NC A:HEM154 2.0 14.8 1.0 NB A:HEM154 2.0 14.8 1.0 NE2 A:HIS93 2.1 9.3 1.0 O A:HOH155 2.1 20.4 1.0 C1D A:HEM154 3.0 9.2 1.0 C4D A:HEM154 3.0 9.3 1.0 C1A A:HEM154 3.0 8.5 1.0 C4C A:HEM154 3.0 8.6 1.0 CE1 A:HIS93 3.0 10.2 1.0 C1C A:HEM154 3.0 8.0 1.0 C4B A:HEM154 3.0 7.3 1.0 C4A A:HEM154 3.0 7.7 1.0 C1B A:HEM154 3.0 7.6 1.0 CD2 A:HIS93 3.1 10.0 1.0 CHD A:HEM154 3.4 8.7 1.0 CHA A:HEM154 3.4 8.7 1.0 CHC A:HEM154 3.4 8.0 1.0 CHB A:HEM154 3.4 7.6 1.0 ND1 A:HIS93 4.2 10.3 1.0 CG A:HIS93 4.2 10.1 1.0 C2D A:HEM154 4.2 9.6 1.0 C3D A:HEM154 4.2 10.1 1.0 C2A A:HEM154 4.3 8.6 1.0 C3A A:HEM154 4.3 8.3 1.0 C3C A:HEM154 4.3 9.3 1.0 C2C A:HEM154 4.3 8.8 1.0 C3B A:HEM154 4.3 7.7 1.0 C2B A:HEM154 4.3 7.4 1.0 O A:HOH156 4.4 20.6 0.9 ND2 A:ASN68 4.5 16.9 1.0

R.A.Goldbeck, M.L.Pillsbury, R.A.Jensen, J.L.Mendoza, R.L.Nguyen, J.S.Olson, J.Soman, D.S.Kliger, R.M.Esquerra. Optical Detection of Disordered Water Within A Protein Cavity. J.Am.Chem.Soc. V. 131 12265 2009.
ISSN: ISSN 0002-7863
PubMed: 19655795
DOI: 10.1021/JA903409J